2hy6

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PDB ID 2hy6

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, resolution 1.25Å
Ligands:
Gene: GCN4, AAS3, ARG9 (Saccharomyces cerevisiae)
Related: 2ZTA, 1GCM, 1GCL, 2B1F, 2B22


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



A seven-helix coiled coil


Overview

Coiled-coil proteins contain a characteristic seven-residue sequence repeat whose positions are designated a to g. The interacting surface between alpha-helices in a classical coiled coil is formed by interspersing nonpolar side chains at the a and d positions with hydrophilic residues at the flanking e and g positions. To explore how the chemical nature of these core amino acids dictates the overall coiled-coil architecture, we replaced all eight e and g residues in the GCN4 leucine zipper with nonpolar alanine side chains. Surprisingly, the alanine-containing mutant forms a stable alpha-helical heptamer in aqueous solution. The 1.25-A resolution crystal structure of the heptamer reveals a parallel seven-stranded coiled coil enclosing a large tubular channel with an unusual heptad register shift between adjacent staggered helices. The overall geometry comprises two interleaved hydrophobic helical screws of interacting cross-sectional a and d layers that have not been seen before. Moreover, asparagines at the a positions play an essential role in heptamer formation by participating in a set of buried interhelix hydrogen bonds. These results demonstrate that heptad repeats containing four hydrophobic positions can direct assembly of complex, higher-order coiled-coil structures with rich diversity for close packing of alpha-helices.

About this Structure

2HY6 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

A seven-helix coiled coil., Liu J, Zheng Q, Deng Y, Cheng CS, Kallenbach NR, Lu M, Proc Natl Acad Sci U S A. 2006 Oct 17;103(42):15457-62. Epub 2006 Oct 9. PMID:17030805

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